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UniProtKB/Swiss-Prot entry P37172


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACVR1_MOUSE
Primary accession number P37172
Secondary accession numbers Q3UDH5 Q91VF1
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on October 17, 2006 (Sequence version 2)
Annotations were last modified on    June 10, 2008 (Entry version 81)
Name and origin of the protein
Protein name Activin receptor type-1 [Precursor]
Synonyms EC 2.7.11.30
Activin receptor type I
ACTR-I
Serine/threonine-protein kinase receptor R1
SKR1
TGF-B superfamily receptor type I
TSR-I
TSK-7L
Gene name
Name: Acvr1
Synonyms: Acvrlk2, Tgfb1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=8388127 [NCBI, ExPASy, EBI, Israel, Japan]
Ebner R., Chen H., Shum L., Lawler S., Lee A.L., Zioncheck T.F., Lopez A.R., Derynck R.;
"Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor.";
Science 260:1344-1348(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ILS, and ISS;
DOI=10.1007/s00335-001-1001-x; PubMed=11471062 [NCBI, ExPASy, EBI, Israel, Japan]
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
"High-throughput sequence identification of gene coding variants within alcohol-related QTLs.";
Mamm. Genome 12:657-663(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Bone marrow;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6;
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DEVELOPMENTAL STAGE, AND FUNCTION.
DOI=10.1016/j.ydbio.2004.08.042; PubMed=15531373 [NCBI, ExPASy, EBI, Israel, Japan]
Kishigami S., Yoshikawa S., Castranio T., Okazaki K., Furuta Y., Mishina Y.;
"BMP signaling through ACVRI is required for left-right patterning in the early mouse embryo.";
Dev. Biol. 276:185-193(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L15436; AAA40495.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF332087; AAK56115.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF332088; AAK56116.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK150014; BAE29239.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK150075; BAE29286.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058718; AAH58718.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A37489; I59576.
RefSeq NP_001103674.1; -.
NP_001103675.1; -.
NP_031420.2; -.
UniGene Mm.689
3D structure databases
HSSP P36897; 1IAS. [HSSP ENTRY / PDB]
ModBase P37172.
Protein-protein interaction databases
DIP DIP:5798N; -.
Organism-specific databases
MGI MGI:87911; Acvr1.
GeneLynx Acvr1; Mus musculus.
Gene expression databases
ArrayExpress P37172; -.
CleanEx MM_ACVR1; -.
MM_TGFB1; -.
GermOnline ENSMUSG00000026836; Mus musculus.
Ontologies
GO
GO:0045177; Cellular component: apical part of cell (inferred from direct assay from MGI).
GO:0005887; Cellular component: integral to plasma membrane (inferred from direct assay from MGI).
GO:0048185; Molecular function: activin binding (inferred from physical interaction from MGI).
GO:0016361; Molecular function: activin receptor activity, type I (inferred from direct assay from MGI).
GO:0050431; Molecular function: transforming growth factor beta binding (inferred from direct assay from MGI).
GO:0002526; Biological process: acute inflammatory response (inferred from expression pattern from UniProtKB).
GO:0007368; Biological process: determination of left/right symmetry (inferred from mutant phenotype from MGI).
GO:0001702; Biological process: gastrulation with mouth forming second (inferred from mutant phenotype from MGI).
GO:0007281; Biological process: germ cell development (inferred from mutant phenotype from MGI).
GO:0007507; Biological process: heart development (inferred from mutant phenotype from MGI).
GO:0001701; Biological process: in utero embryonic development (inferred from mutant phenotype from MGI).
GO:0001707; Biological process: mesoderm formation (inferred from mutant phenotype from MGI).
GO:0001755; Biological process: neural crest cell migration (inferred from mutant phenotype from MGI).
GO:0001569; Biological process: patterning of blood vessels (inferred from mutant phenotype from MGI).
GO:0060037; Biological process: pharyngeal system development (inferred from mutant phenotype from MGI).
GO:0051145; Biological process: smooth muscle cell differentiation (inferred from mutant phenotype from MGI).
GO:0007179; Biological process: transforming growth factor beta receptor signaling pathway (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000333; Activin_II_recpt.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR008271; Ser_thr_pkin_AS.
IPR003605; TGF_beta_rcpt_GS.
Graphical view of domain structure.
Pfam PF01064; Activin_recp; 1.
PF08515; TGF_beta_GS; 1.
Pfam graphical view of domain structure.
PRINTS PR00653; ACTIVIN2R.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00467; GS; 1.
SMART graphical view of domain structure.
PROSITE PS51256; GS; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P37172.
Genome annotation databases
Ensembl ENSMUSG00000026836; Mus musculus. [Contig view]
GeneID 11477; -.
KEGG mmu:11477; -.
Phylogenomic databases
HOGENOM P37172; -.
HOVERGEN P37172; -.
Other
SOURCE Acvr1; Mus musculus.
ProtoNet P37172.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     By similarity. 
CHAIN   21   509  489     Activin receptor type-1. PRO_0000024395
TOPO_DOM   21   123  103     Extracellular (Potential). 
TRANSMEM   124   146  23     Potential. 
TOPO_DOM   147   509  363     Cytoplasmic (Potential). 
DOMAIN   178   207  30     GS. 
DOMAIN   208   502  295     Protein kinase. 
NP_BIND   214   222  9     ATP (By similarity). 
ACT_SITE   336   336        Proton acceptor (By similarity). 
BINDING   235   235        ATP (By similarity). 
MOD_RES   501   501        Phosphoserine (By similarity). 
CARBOHYD   102   102        N-linked (GlcNAc...) (Potential). 
CONFLICT   27    27        K -> E (in Ref. 3; BAE29239/BAE29286). 
CONFLICT   60    60        N -> Y (in Ref. 1; AAA40495). 
Sequence information
Length: 509 AA [This is the length of the unprocessed precursor] Molecular weight: 57226 Da [This is the MW of the unprocessed precursor] CRC64: 05BCFC22C5740028 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVDGVMILPV LMMMAFPSPS VEDEKPKVNQ KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN 

        70         80         90        100        110        120 
DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF 

       130        140        150        160        170        180 
HLEVGLIILS VVFAVCLLAC ILGVALRKFK RRNQERLNPR DVEYGTIEGL ITTNVGDSTL 

       190        200        210        220        230        240 
AELLDHSCTS GSGSGLPFLV QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR 

       250        260        270        280        290        300 
DEKSWFRETE LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL 

       310        320        330        340        350        360 
DTVSCLRIVL SIASGLAHLH IEIFGTQGKS AIAHRDLKSK NILVKKNGQC CIADLGLAVM 

       370        380        390        400        410        420 
HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK RVDIWAFGLV LWEVARRMVS 

       430        440        450        460        470        480 
NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ 

       490        500 
NPSARLTALR IKKTLTKIDN SLDKLKTDC 

P37172 in FASTA format

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